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Database: UniProt
Entry: F0X8G2_GROCL
LinkDB: F0X8G2_GROCL
Original site: F0X8G2_GROCL 
ID   F0X8G2_GROCL            Unreviewed;       625 AA.
AC   F0X8G2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EFX05262.1};
GN   ORFNames=CMQ_3331 {ECO:0000313|EMBL:EFX05262.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX05262.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; GL629735; EFX05262.1; -; Genomic_DNA.
DR   RefSeq; XP_014174744.1; XM_014319269.1.
DR   AlphaFoldDB; F0X8G2; -.
DR   STRING; 655863.F0X8G2; -.
DR   GeneID; 25976420; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_2_1; -.
DR   InParanoid; F0X8G2; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT   DOMAIN          296..310
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         245
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   625 AA;  66968 MW;  F5A22B7E00AE9E78 CRC64;
     MGSTGEDQAA TFDYIIAGGG TAGVVVAARL SEDPSIKVLL IEAGADHSKD PLVLTPGLVA
     GVYGKKEYDW NFSSVPQPTL HGRAINQARG RMLGGCSGIN FMMAVYPSRA ILDAWGALGN
     KGWSFDELEP YFRKFATTEP PSALTTSTCR VAGHYDDAIT QTETGPLQIS YGEGHSPNNS
     AWFDTFANLG LRMTSDPRGG SAVGAFQNTA TIDPKTKTRS FAVTAYLTEK VLARTNLTIW
     TEAVVTKILL ESPSAHTADP DVVAVAKGVR VRSGNGGETG KERDVFARAE VILAAGTLQT
     PQLLELSGIG GRDILEKHAI PVVVDNPNVG EHLQDHAVVC QSFEVAPGTL SGDILRDPDL
     LNALVQQYQT DGQGPMGQSA ISCAYAPLLD ADGPLSAEAR QAFFDAHSDS GEEEHGLVRK
     LLSGPGEPSV QFLLFPTQVS IRKNPSSMAE IIVPSQPENY LTIMSVLNHP FSRGQVHITS
     GNIDDLPVWD PHYNSESIDM EILARAVRFV ETFAYTKPFA GLLMPPGEGK RMPDICADDL
     DQAREIVRQA QISIFHVCGS CVMKPKDKGG VVDGKLRVYG VSNLRIVDAS IFPIEPLGNI
     QTTVYAVAEK AADIIKQGRQ GHSSN
//
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